Source:http://linkedlifedata.com/resource/pubmed/id/10758001
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
|
| pubmed:dateCreated |
2000-6-16
|
| pubmed:abstractText |
Maltose permease is required for maltose transport into Saccharomyces cells. Glucose addition to maltose-fermenting cells causes selective delivery of this integral plasma membrane protein to the yeast vacuole via endocytosis for degradation by resident proteases. This glucose-induced degradation is independent of the proteasome but requires ubiquitin and certain ubiquitin conjugating enzymes. We used mutation analysis to identify target sequences in Mal61/HA maltose permease involved in its selective glucose-induced degradation. A nonsense mutation was introduced at codon 581, creating a truncated functional maltose permease. Additional missense mutations were introduced into the mal61/HA-581NS allele, altering potential phosphorylation and ubiquitination sites. No significant effect was seen on the rate of glucose-induced degradation of these mutant proteins. Deletion mutations were constructed, removing residues 2-30, 31-60, 61-90, and 49-78 of the N-terminal cytoplasmic domain, as well as a missense mutation of a dileucine motif. Results indicate that the proline-, glutamate-, aspartate-, serine-, and threonine-rich (PEST) sequence found in the N-terminal cytoplasmic domain, particularly residues 49-78, is required for glucose-induced degradation of Mal61/HAp and for the rapid glucose-induced inactivation of maltose transport activity. The decreased rate of glucose-induced degradation correlates with a decrease in the level of glucose-induced ubiquitination of the DeltaPEST mutant permease. In addition, newly synthesized mutant permease proteins lacking residues 49-78 or carrying an alteration in the dileucine motif, residues 69 and 70, are resistant to glucose-induced inactivation of maltose transport activity. This N-terminal PEST-like sequence is the target of both the Rgt2p-dependent and the Glc7p-Reg1p-dependent glucose signaling pathways.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RGT2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/maltose permease,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, S...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
18
|
| pubmed:volume |
39
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4518-26
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:10758001-Amino Acid Motifs,
pubmed-meshheading:10758001-Amino Acid Sequence,
pubmed-meshheading:10758001-Amino Acid Substitution,
pubmed-meshheading:10758001-Biological Transport,
pubmed-meshheading:10758001-Carrier Proteins,
pubmed-meshheading:10758001-Fermentation,
pubmed-meshheading:10758001-Fungal Proteins,
pubmed-meshheading:10758001-Glucose,
pubmed-meshheading:10758001-Half-Life,
pubmed-meshheading:10758001-Leucine,
pubmed-meshheading:10758001-Maltose,
pubmed-meshheading:10758001-Membrane Proteins,
pubmed-meshheading:10758001-Membrane Transport Proteins,
pubmed-meshheading:10758001-Molecular Sequence Data,
pubmed-meshheading:10758001-Monosaccharide Transport Proteins,
pubmed-meshheading:10758001-Protein Structure, Tertiary,
pubmed-meshheading:10758001-Saccharomyces cerevisiae,
pubmed-meshheading:10758001-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10758001-Sequence Deletion,
pubmed-meshheading:10758001-Signal Transduction,
pubmed-meshheading:10758001-Symporters,
pubmed-meshheading:10758001-Ubiquitins
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
A PEST-like sequence in the N-terminal cytoplasmic domain of Saccharomyces maltose permease is required for glucose-induced proteolysis and rapid inactivation of transport activity.
|
| pubmed:affiliation |
Biology Department, Queens College and the Graduate School of the City University of New York, 65-30 Kissena Boulevard, Flushing, New York 11367, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|